I gu,erfdi g-iXcln-yYe is necitlchlya dceerodisn a yaprirm“ oimna icda tcurusetr of a n”toprie esicn teh detiinnfoi of a rarPmiy ecrrsttuu of a nprioet si a“ rainle incah fo namoi cas.di” fI uyo sesm hiwt hte Pirrmya trtcers,uu as ni the eiotnuqs ,tsem ouy ctnnao omrf the ayroeSndc csutrretu fo hte roinpt,e hwich is mdreitdnee by het -rydgnonedigbnho hwhic cuorcs beetnwe hte pitedep obbaknec, iedptnednne fo the R p.ursog I hpeo hsit adme es.nes
orFm dawiiekip: dc“reaSony tsrcruuet si oylrlfam iefdden yb eth eptrnat fo dnrehgyo nbods tebenew hte imnoa ngydhreo dna labyrcox eynogx smato ni hte dieppte ckbabeon”. phms(esia men)i
From Molecular Biology of the Cell:
Biologists distinguish four levels of organization in the structure of a protein. The amino acid sequence is known as the primary structure of the protein. Stretches of polypeptide chain that form α helices and β sheets constitute the protein’s secondary structure. The full three-dimensional organization of a polypeptide chain is sometimes referred to as the protein’s tertiary structure, and if a particular protein molecule is formed as a complex of more than one polypeptide chain, the complete structure is designated as the quaternary structure.
ko ygsu adn i qteou rfom ecsaostw1e/hu4so//esmarttdrhsp/et/i0iomws-ooctepbltwe.rgn.:2ecpilfit
%"90 avhe na fbilietnaied gtniece oittnuam O
CL 11A nad LCO 12A
ceauss
brmaolan alglecon lorgns-isiknc avi a clengiy tsibouisttnu ni eth palnrgoloec llemueco "
hcwih aensm taht IO sah a licgeny itnuobiutsst dna eohfrert ist luneab to rmof a osecyndra et.truusrcu
eDu ot cgielnys' lsmal i,zes it trcseea ks""kin in eth maino diac c.qeeseun sThee isnkk are deneed ot ecrtlcroy omrf het scynreoad strturuce.
hOret wsasrn:e
y-lGY-X si nakbbeco orf aocnlleg ahapl a.hnci 3 oaenllcg plhaa hcansi lirsap ot orfm trlpie .ixhle ilcyGne sah no R ur,gpo onaliwlg rof xltiliyfieb dan ftiaomrno of liretp .helxi No cnlgiey nsertpve hsti inuocnstou rl,piigsna veneitgnpr hte ioamotfnr of agcllone scnoardye erutucs.rt
Ralcel htat lhecalhi-pase and hstse-bteea era eaxspmle fo asnoydcre cssruttur.e hsiT anc be hgttuho of a emonntiitsafa of eht ahpal hl.xie
htreANo wya ot gte at ti si avi oniei:alintm
A. engryhod iodgnnb tlonwdu ylaelr acehgn ceisn tnerhie eaainnl nor nyclegi aer Bol apr. yGl t;g& Aal oht'nlsdu necagh woh ieonrlp si eofdidmi (I eanm it OUD,CL if hteer swa a etscir haneirdnc ro ,sitnohegm btu ton a garte r .aewDs)n ohnigtn ot cieiatnd tath lcognlea nregidtedoa is elrtaed ni npsroees ot na AA tinuuistst.bo Al,so in eth tcetonx of IO hihwc( is hte nsnigrpeet an,tlio)mpc ew aldeyra wonk tath teh ebmprlo eodn'st veah nhanygit to od with edidnoegrat, omre iwht teh cgeahn in rnucnu tfseEuo/ctitr. nltsyHoe dnt'o wnko.
e’serH eon wya to rpaeesom-icne-itlfso ercs“aeedd enbh-rdgdyono i”:tronomfa mI’ not a igb naf fo shit lein of snenrig,oa btu alenctclhyi ielaann sa a edsi ugorp has mreo es*rgondyh rof tpleotnia rhnygode ndibogn athn yeilncg:
anl:aeni 3HC—
:yecnlig —H
,oS t,yaclel“nhci” aaneiln luwdo tmrepi erom dnyd-rohbenog an,ootirmf hichw htimg wlola uyo to enaliemti taht c.eoich
htTa adi,s it semse lomast imospsebil to rule otu wuhtt(io rvye itccanehl ngkwoleed or eoms oiddepvr pertelxaemni )adta ttha hte lgyslhit rlgear ilannea odes ton maprii gynoehdr ogdbinn eneebtw lanlocge eloesmcul aiv srtiec s(aai)plt rrfcntenieee. nI mlrisep t,semr csnie nlenaai si a,lrgre uyo wuold hntik taht it tums oosmehw efrrietne twhi teh odhnoggyr-bnined taht roccsu wtih het weytidl-p nylegci.
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*iyrtlSct pigsekn,a tsi’ ton eht munreb fo hdyrnoesg utb osal eth nsthgrte fo eth edlopi htat aiaetlcstif heoyndrg nbgoid:n a rhnogeyd dunbo ot a ygtrnlos ctorvegeatnleie lmoeeluc like nrolueif llwi p“”epaar erom ieovstpi ,adn h,uts hdg-rnobyedon moer nsrtglyo ithw a yerbna noxyge ocdpm(are twih a ehnogdyr dcnntceeo to ,braonc fro elempx.)a
Fhtreru irgand:e
From Molecular Biology of the Cell:
Hydroxylysines and hydroxyprolines are infrequently found in other animal proteins, although hydroxyproline is abundant in some proteins in the plant cell wall. In collagen, the hydroxyl groups of these amino acids are thought to form interchain hydrogen bonds that help stabilize the triple-stranded helix. Conditions that prevent proline hydroxylation, such as a deficiency of ascorbic acid (vitamin C), have serious consequences. (Emphasis mine)
From Molecular Biology of the Cell:
The primary feature of a typical collagen molecule is its long, stiff, triple-stranded helical structure, in which three collagen polypeptide chains, called α chains, are wound around one another in a ropelike superhelix (Figure 19-43). Collagens are extremely rich in proline and glycine, both of which are important in the formation of the triple-stranded helix. Proline, because of its ring structure, stabilizes the helical conformation in each α chain, while glycine is regularly spaced at every third residue throughout the central region of the α chain. Being the smallest amino acid (having only a hydrogen atom as a side chain), glycine allows the three helical α chains to pack tightly together to form the final collagen superhelix (see Figure 19-43).
I gmhti eb rgnotenhviki it ut,b H obnd iontrfamo fo 'saa smkae het ndrsoeayc uurcretst fo teh pteonir naloclg(e ni thsi .aesc) The Gly ot Aal titusnuisbto sode sleutr ni sesl H nobd ormatifno, btu of dviuilniad aa's ton ewbetne oaclleng oleuelmcs at(th tmgih eb moer fro aqayeruntr e)ctutrsur
riaPymr urttsurec = inoma caid yeunrqeSecoenadcs srrecutut = usutetcrr rfmdoe ihwt a ilgsen omnai icad eqsuneec taeb( tepadle te,she lpaha l,hexi teycraietr T) setrucurt = tlumlepi oadsecryn trtrsueucs aitrcetnign gothtree lutil(pme tbea taleepd seeths cadestk on tpo fo haec o,rhte r enruetatyaQ)cr sucrrutte = ioneptr tsreucurt fomedr romf ofligdn of all riattyer rusctstrue ot eakm ndnibig i,ests ce.t
Scnei het linaena saw utp in plaec fo eth eyGcn,li hte mryairp ctruutser was lnaebu ot fmor na ahpla ilxeh seinc ahlap xileh sutsrcuter edne a auctrrpail neqcseue y(gl - x- y) ni rerdo ot form ngryhdeo nbsod to keep teh ehilx tesbal.
thwa si nlelcoga ? a ecryaodns oprneti .cruetsutr
nehw uoy mveero line,cgy eth omst dutnbaan naiom idca , from the rucoprres eeocllum ilwl uoy etg a eprrop edonrcsay eurtrtsuc ? NO
lGy si r,palo eAnianl is ornlopna nad iohypocrd.bh ssMneies ntcsoonnreevaiv at.toimun Thees sAA have fditenfer malciehc estiropper cwihh aled to updtiersd rtnieop londgif ancoryse(d )trrcuteu.s imaSrli to Gul - lVa uttinobiusst ni ceSikl llCe eassDie.
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$279$49I thkin ti ash hginmteos ot od hitw ecigyln du(e to ist allsm isez ti nac tif in namy eslpac wheer ertoh aionm sdica cna nto dan eenhc ti deorvisp lrut“cuastr pecos”namtcs ot het lceognla, ie.. tup a iknk ni eht ahlpa .hxil)e fI niygelc si ecadiplsm by mtiosehng ees,l I o’tdn knith glopn-rlecoa can rmfo tis trocrce sacyednor .urtrecuts
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